Purification and characterization of xylanases from Aspergillus giganteus
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15114860
DOI
10.1007/bf02931639
Knihovny.cz E-resources
- MeSH
- Enzyme Activators analysis pharmacology MeSH
- Aspergillus enzymology growth & development MeSH
- Dextrans MeSH
- Dithiothreitol MeSH
- Sodium Dodecyl Sulfate MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Endo-1,4-beta Xylanases chemistry isolation & purification metabolism MeSH
- Fractional Precipitation MeSH
- Fungal Proteins chemistry isolation & purification metabolism MeSH
- Chromatography, Gel MeSH
- Glycoproteins chemistry isolation & purification metabolism MeSH
- Enzyme Inhibitors analysis pharmacology MeSH
- Kinetics MeSH
- Hydrogen-Ion Concentration MeSH
- Culture Media chemistry MeSH
- Copper analysis pharmacology MeSH
- Molecular Weight MeSH
- Ammonium Sulfate chemistry MeSH
- Mercury Compounds analysis pharmacology MeSH
- Enzyme Stability MeSH
- Substrate Specificity MeSH
- Temperature MeSH
- Xylans metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Enzyme Activators MeSH
- Dextrans MeSH
- Dithiothreitol MeSH
- Sodium Dodecyl Sulfate MeSH
- Endo-1,4-beta Xylanases MeSH
- Fungal Proteins MeSH
- Glycoproteins MeSH
- Enzyme Inhibitors MeSH
- Culture Media MeSH
- Copper MeSH
- sephadex MeSH Browser
- Ammonium Sulfate MeSH
- Mercury Compounds MeSH
- Xylans MeSH
A strain of Aspergillus giganteus cultivated in a medium with xylan produced two xylanases (xylanase I and II) which were purified to homogeneity. Their molar mass, estimated by SDS-PAGE, were 21 and 24 kDa, respectively. Both enzymes are glycoproteins with 50 degrees C temperature optimum; optimum pH was 6.0-6.5 for xylanase I and 6.0 for xylanase II. At 50 degrees C xylanase I exhibited higher thermostability than xylanase II. Hg2+, Cu2+ and SDS were strong inhibitors, 1,4-dithiothreitol stimulated the reaction of both enzymes. Both xylanases are xylan-specific; kinetic parameters indicated higher efficiency in the hydrolysis of oat spelts xylan. In hydrolysis of this substrate, xylotriose, xylotetraose and larger xylooligosaccharides were released and hence the enzymes were classified as endoxylanases.
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